ID A0A401SSA7_CHIPU Unreviewed; 591 AA.
AC A0A401SSA7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=HTH CENPB-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=chiPu_0011724 {ECO:0000313|EMBL:GCC33256.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC33256.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC33256.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyoctanoate + O2 = 2-oxooctanoate + H2O2;
CC Xref=Rhea:RHEA:67940, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:133514, ChEBI:CHEBI:176689;
CC Evidence={ECO:0000256|ARBA:ARBA00029327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67941;
CC Evidence={ECO:0000256|ARBA:ARBA00029327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2;
CC Xref=Rhea:RHEA:16789, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:35179, ChEBI:CHEBI:58123; EC=1.1.3.15;
CC Evidence={ECO:0000256|ARBA:ARBA00029325};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790;
CC Evidence={ECO:0000256|ARBA:ARBA00029325};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC33256.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BEZZ01000499; GCC33256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401SSA7; -.
DR STRING; 137246.A0A401SSA7; -.
DR OMA; PIFANIW; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProt.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR PANTHER; PTHR10578:SF139; 2-HYDROXYACID OXIDASE 2; 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR SMART; SM00674; CENPB; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
DR PROSITE; PS51253; HTH_CENPB; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033}.
FT DOMAIN 31..106
FT /note="HTH CENPB-type"
FT /evidence="ECO:0000259|PROSITE:PS51253"
FT DOMAIN 233..591
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
SQ SEQUENCE 591 AA; 66879 MW; 8009B50A6B636147 CRC64;
MQYDMAKSTI CTILKNKQTL KAADVAKGVT ILMKQRPKLL DDVEKLLLVW INQKELAGDS
VDEICWRHRD LLATPPSTST ARVEEFKASR GWFDKFRRRT GIHSVIRHGE AASSDKKAAE
DFVKEFNKFV EDEGHVSYQS AWRKLWPDCE PERDFEGFEE ETSVNVVNEI MTLGQNIGLE
VNEDDVVELV EDHKQKLSIE DLVELQQEQW KSHEQARRAT EIGIFAIRSS LCDPEMSLVC
LSDFEVYAKE HLPKTTWDYY AAGADECCTR DDNLMAYKRI RLRPRMLRDV SVTDTRVTIQ
GMEISFPIGI APTAFHCMAW HDGEMSTARA AEAMNTCYIA STYSTCSVEE ISAAAPNGFR
WFQLYVYRNR KLSEQLVHRV EAHGYKAIVL TVDVPYTGKR RNDIRNNFKL PPHLKVKNFD
GIFEDHSEVE LYGVPANSLD PSICWKDICW LQSLTRLPII IKGILTKEDA ELAVEHGVQG
IIVSNHGGRQ LDGGPATIDA LSEIVDTVQG RIEVYLDGGI RTGSDVLKAL AIGAKCVFIG
RPVVWGLVYK GEEGVKEILQ ILNDEFRLSM ALAGCRNISE INRNLVQFSK L
//
